Use of monolithic supports for high-throughput protein and peptide separation in proteomics
Апстракт
The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biologica...l samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.
Кључне речи:
High-throughput / Liquid chromatography / Mass spectrometry / Monoliths / ProteomicsИзвор:
Electrophoresis, 2017, 38, 22-23, 2851-2869Издавач:
- Wiley, Hoboken
Финансирање / пројекти:
- Производња, изоловање и карактеризација ензима и малих молекула и њихова примена у растворном и имобилизованом облику у биотехнологији хране, биогоривима и заштитити животне средине (RS-MESTD-Basic Research (BR or ON)-172048)
- Интеракције природних производа, њихових деривата и комплексних једињења са протеинима и нуклеинским киселинама (RS-MESTD-Basic Research (BR or ON)-172055)
- Алергени, антитела, ензими и мали физиолошки значајни молекули: дизајн, структура, функција и значај (RS-MESTD-Basic Research (BR or ON)-172049)
- HTP-GLYCOMET - Methods for high-throughput glycoproteomic analysis (EU-FP7-324400)
Напомена:
- This is the peer-reviewed version of the following article:Andjelkovic, U.; Tufegdzic, S.; Popović, M. Use of Monolithic Supports for High-Throughput Protein and Peptide Separation in Proteomics. Electrophoresis 2017, 38 (22–23), 2851–2869, https://dx.doi.org/10.1002/elps.201700260
- http://cer.ihtm.bg.ac.rs/handle/123456789/2122
DOI: 10.1002/elps.201700260
ISSN: 0173-0835
PubMed: 28906564
WoS: 000416867300006
Scopus: 2-s2.0-85036597546
Институција/група
IHTMTY - JOUR AU - Anđelković, Uroš AU - Tufegdžić, Srđan AU - Popović, Milica PY - 2017 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/2985 AB - The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed. PB - Wiley, Hoboken T2 - Electrophoresis T1 - Use of monolithic supports for high-throughput protein and peptide separation in proteomics VL - 38 IS - 22-23 SP - 2851 EP - 2869 DO - 10.1002/elps.201700260 ER -
@article{ author = "Anđelković, Uroš and Tufegdžić, Srđan and Popović, Milica", year = "2017", abstract = "The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.", publisher = "Wiley, Hoboken", journal = "Electrophoresis", title = "Use of monolithic supports for high-throughput protein and peptide separation in proteomics", volume = "38", number = "22-23", pages = "2851-2869", doi = "10.1002/elps.201700260" }
Anđelković, U., Tufegdžić, S.,& Popović, M.. (2017). Use of monolithic supports for high-throughput protein and peptide separation in proteomics. in Electrophoresis Wiley, Hoboken., 38(22-23), 2851-2869. https://doi.org/10.1002/elps.201700260
Anđelković U, Tufegdžić S, Popović M. Use of monolithic supports for high-throughput protein and peptide separation in proteomics. in Electrophoresis. 2017;38(22-23):2851-2869. doi:10.1002/elps.201700260 .
Anđelković, Uroš, Tufegdžić, Srđan, Popović, Milica, "Use of monolithic supports for high-throughput protein and peptide separation in proteomics" in Electrophoresis, 38, no. 22-23 (2017):2851-2869, https://doi.org/10.1002/elps.201700260 . .